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Literature summary for 4.2.1.1 extracted from

  • Jewell, D.A.; Tu, C.; Paranawithana, S.R.; Tanhauser, S.M.; LoGrasso, P.V.; Laipis, P.J.; Silverman, D.N.
    Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesis (1991), Biochemistry, 30, 1484-1490.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K64H mutant of carbonic anhydrase III, pH-dependent behavior and enhanced CO2 hydration activity compared to the wild-type enzyme, no enhanced hydrolysis rate Homo sapiens
R67N mutant of carbonic anhydrase III, pH-dependent behavior and enhanced CO2 hydration activity compared to the wild-type enzyme, no enhanced hydrolysis rate Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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carbonic anhydrase III
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO2 + H2O among the seven known isozymes carbonic anhydrase III is the least efficient in catalytic hydration of CO2 Homo sapiens H2CO3
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r